Parkin Regulates the Activity of Pyruvate Kinase M2
Parkin, a ubiquitin E3 ligase, is mutated in most cases of autosomal recessive early onset Parkinson disease. It was discovered that Parkin is also mutated in glioblastoma and other human malignancies and that it inhibits tumor cell growth. Here, we identified pyruvate kinase M2 (PKM2) as a unique s...
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| Published in | The Journal of biological chemistry Vol. 291; no. 19; pp. 10307 - 10317 |
|---|---|
| Main Authors | , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Elsevier Inc
06.05.2016
American Society for Biochemistry and Molecular Biology |
| Subjects | |
| Online Access | Get full text |
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| Abstract | Parkin, a ubiquitin E3 ligase, is mutated in most cases of autosomal recessive early onset Parkinson disease. It was discovered that Parkin is also mutated in glioblastoma and other human malignancies and that it inhibits tumor cell growth. Here, we identified pyruvate kinase M2 (PKM2) as a unique substrate for parkin through biochemical purification. We found that parkin interacts with PKM2 both in vitro and in vivo, and this interaction dramatically increases during glucose starvation. Ubiquitylation of PKM2 by parkin does not affect its stability but decreases its enzymatic activity. Parkin regulates the glycolysis pathway and affects the cell metabolism. Our studies revealed the novel important roles of parkin in tumor cell metabolism and provided new insight for therapy of Parkinson disease. |
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| AbstractList | Parkin, a ubiquitin E3 ligase, is mutated in most cases of autosomal recessive early onset Parkinson disease. It was discovered that Parkin is also mutated in glioblastoma and other human malignancies and that it inhibits tumor cell growth. Here, we identified pyruvate kinase M2 (PKM2) as a unique substrate for parkin through biochemical purification. We found that parkin interacts with PKM2 both in vitro and in vivo, and this interaction dramatically increases during glucose starvation. Ubiquitylation of PKM2 by parkin does not affect its stability but decreases its enzymatic activity. Parkin regulates the glycolysis pathway and affects the cell metabolism. Our studies revealed the novel important roles of parkin in tumor cell metabolism and provided new insight for therapy of Parkinson disease. Parkin, a ubiquitin E3 ligase, is mutated in most cases of autosomal recessive early onset Parkinson disease. It was discovered that Parkin is also mutated in glioblastoma and other human malignancies and that it inhibits tumor cell growth. Here, we identified pyruvate kinase M2 (PKM2) as a unique substrate for parkin through biochemical purification. We found that parkin interacts with PKM2 both in vitro and in vivo , and this interaction dramatically increases during glucose starvation. Ubiquitylation of PKM2 by parkin does not affect its stability but decreases its enzymatic activity. Parkin regulates the glycolysis pathway and affects the cell metabolism. Our studies revealed the novel important roles of parkin in tumor cell metabolism and provided new insight for therapy of Parkinson disease. |
| Author | Luo, Jianyuan Liu, Kun Zheng, Bin Gu, Wei Mao, Zebin Li, Fanzhou Han, Haichao Zhao, Yingming Zhao, Wenhui Chen, Yue |
| Author_xml | – sequence: 1 givenname: Kun surname: Liu fullname: Liu, Kun organization: Department of Biochemistry and Molecular Biology, Peking University Health Science Center and Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, Beijing 100191, China – sequence: 2 givenname: Fanzhou surname: Li fullname: Li, Fanzhou organization: Department of Biochemistry and Molecular Biology, Peking University Health Science Center and Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, Beijing 100191, China – sequence: 3 givenname: Haichao surname: Han fullname: Han, Haichao organization: Department of Biochemistry and Molecular Biology, Peking University Health Science Center and Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, Beijing 100191, China – sequence: 4 givenname: Yue surname: Chen fullname: Chen, Yue organization: Ben May Department of Cancer Research, The University of Chicago, Chicago, Illinois 60637 – sequence: 5 givenname: Zebin surname: Mao fullname: Mao, Zebin organization: Department of Biochemistry and Molecular Biology, Peking University Health Science Center and Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, Beijing 100191, China – sequence: 6 givenname: Jianyuan surname: Luo fullname: Luo, Jianyuan organization: Department of Genetics, Peking University Health Science Center, Beijing 100191, China – sequence: 7 givenname: Yingming surname: Zhao fullname: Zhao, Yingming organization: Ben May Department of Cancer Research, The University of Chicago, Chicago, Illinois 60637 – sequence: 8 givenname: Bin surname: Zheng fullname: Zheng, Bin organization: Cutaneous Biology Research Center, Massachusetts General Hospital, Harvard Medical School, Charlestown, Massachusetts 02129 – sequence: 9 givenname: Wei surname: Gu fullname: Gu, Wei organization: Institute for Cancer Genetics and Department of Pathology and Cell Biology, College of Physicians and Surgeons, Columbia University, New York, New York 10032 – sequence: 10 givenname: Wenhui surname: Zhao fullname: Zhao, Wenhui email: zhao6025729@bjmu.edu.cn organization: Department of Biochemistry and Molecular Biology, Peking University Health Science Center and Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, Beijing 100191, China |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/26975375$$D View this record in MEDLINE/PubMed |
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| Keywords | Parkinson disease ubiquitylation (ubiquitination) parkin glycolysis pyruvate kinase pyruvate kinase M2 |
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| SubjectTerms | Cell Line Glucose - genetics Glucose - metabolism Glycolysis Humans parkin Parkinson disease Parkinson Disease - enzymology Parkinson Disease - genetics Parkinson Disease - pathology pyruvate kinase Pyruvate Kinase - chemistry Pyruvate Kinase - genetics Pyruvate Kinase - metabolism pyruvate kinase M2 Signal Transduction Ubiquitin-Protein Ligases - chemistry Ubiquitin-Protein Ligases - genetics Ubiquitin-Protein Ligases - metabolism Ubiquitination ubiquitylation (ubiquitination) |
| Title | Parkin Regulates the Activity of Pyruvate Kinase M2 |
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